ID Q2LXS9_SYNAS Unreviewed; 683 AA.
AC Q2LXS9;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Molybdopterin dependent oxidoreductase {ECO:0000313|EMBL:ABC78890.1};
GN ORFNames=SYN_01672 {ECO:0000313|EMBL:ABC78890.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78890.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC78890.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC78890.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP000252; ABC78890.1; -; Genomic_DNA.
DR RefSeq; WP_011418906.1; NC_007759.1.
DR AlphaFoldDB; Q2LXS9; -.
DR STRING; 56780.SYN_01672; -.
DR KEGG; sat:SYN_01672; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR InParanoid; Q2LXS9; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000001933; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT DOMAIN 1..54
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
SQ SEQUENCE 683 AA; 75593 MW; DC808599A1DFEACA CRC64;
MQCHTVCRLC SACCPVTVTV EAGKMVRAAR KSFLPEEKRL SCPKLAAAPE IVYSPARILR
PLIRSGPGNG FHEASWDEAL GRVAERFNFF RRTDGAQSIA WLRGMAADWG APWDYACRLM
NAFGSPNTIG NGSVCHVARE MAHAFTYGAM TLPQPRNSRC ILIWGKNDRN TAPGVCEQIL
HARSHGARLI VVDPIRTSFA QMADIWLQIK PGHDGPLAMA MLNEIINNNL YDAAFVDQYG
IGFDELRAAV AHFSPDLVAA DLWLDPEDIR RAARLYATTR PACIIDGNGL DMQLSTFQAT
RAVCMLRAVT GNIDREGGDL IPQPIPLKNI QLKERLPKDV QPVTAAYPLF DAFHPTWGRH
AQSCLIDAIL GERPYPIRML VVQSGNPAVT MTDAKRVRRA LQKLDFLVVI DLFRNRTAEM
ADVILPAASC FEKTQLNRAS MRSSPVVLQN QVIDCLGESR PDWQIVFELG RRLGLEADFP
WASVEAAIDE QLSPSGLTVA FLRENPDGLW TEPTKFEKYR SKGFATPSGR VEFHSDRLAR
AGHAPVPFAE GTFEDLPGSA DACNADVVIG ISGERTNRFT HTQFLRIPSL ARQEPEGFVD
IHPRDAAARG ISDGQEITIS NERGQVRMKA RISDVVHPGS IRIAWGWGEI DPDANVNNLT
DDNRRDPITA TPSNRSFLCR IET
//
